1m8p: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m8p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M8P FirstGlance]. <br> | <table><tr><td colspan='2'>[[1m8p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M8P FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PPS:3-PHOSPHATE-ADENOSINE-5-PHOSPHATE+SULFATE'>PPS</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i2d|1i2d]], [[1g8g|1g8g]], [[1jhd|1jhd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i2d|1i2d]], [[1g8g|1g8g]], [[1jhd|1jhd]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfate_adenylyltransferase Sulfate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.4 2.7.7.4] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m8p RCSB], [http://www.ebi.ac.uk/pdbsum/1m8p PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m8p RCSB], [http://www.ebi.ac.uk/pdbsum/1m8p PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/MET3_PENCH MET3_PENCH]] Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Penicillium chrysogenum]] | [[Category: Penicillium chrysogenum]] | ||
[[Category: Sulfate adenylyltransferase]] | [[Category: Sulfate adenylyltransferase]] | ||
[[Category: Fisher, A J | [[Category: Fisher, A J]] | ||
[[Category: MacRae, I J | [[Category: MacRae, I J]] | ||
[[Category: Segel, I H | [[Category: Segel, I H]] | ||
[[Category: Phosphosulfate binding]] | [[Category: Phosphosulfate binding]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
[[Category: T-state]] | [[Category: T-state]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
